1lfp: Difference between revisions
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<StructureSection load='1lfp' size='340' side='right' caption='[[1lfp]], [[Resolution|resolution]] 1.72Å' scene=''> | <StructureSection load='1lfp' size='340' side='right' caption='[[1lfp]], [[Resolution|resolution]] 1.72Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1lfp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1lfp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LFP FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lfp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lfp RCSB], [http://www.ebi.ac.uk/pdbsum/1lfp PDBsum], [http://www.topsan.org/Proteins/BSGC/1lfp TOPSAN]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lfp OCA], [http://pdbe.org/1lfp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lfp RCSB], [http://www.ebi.ac.uk/pdbsum/1lfp PDBsum], [http://www.topsan.org/Proteins/BSGC/1lfp TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1lfp" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aquifex aeolicus]] | [[Category: Aquifex aeolicus huber and stetter 2001]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Kim, R]] | [[Category: Kim, R]] | ||
Revision as of 04:29, 10 September 2015
Crystal Structure of a Conserved Hypothetical Protein Aq1575 from Aquifex AeolicusCrystal Structure of a Conserved Hypothetical Protein Aq1575 from Aquifex Aeolicus
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of a conserved hypothetical protein, Aq1575, from Aquifex aeolicus has been determined by using x-ray crystallography. The protein belongs to the domain of unknown function DUF28 in the Pfam and PALI databases for which there was no structural information available until now. A structural homology search with the DALI algorithm indicates that this protein has a new fold with no obvious similarity to those of other proteins of known three-dimensional structure. The protein reveals a monomer consisting of three domains arranged along a pseudo threefold symmetry axis. There is a large cleft with approximate dimensions of 10 A x 10 A x 20 A in the center of the three domains along the symmetry axis. Two possible active sites are suggested based on the structure and multiple sequence alignment. There are several highly conserved residues in these putative active sites. The structure based molecular properties and thermostability of the protein are discussed. Crystal structure of conserved hypothetical protein Aq1575 from Aquifex aeolicus.,Shin DH, Yokota H, Kim R, Kim SH Proc Natl Acad Sci U S A. 2002 Jun 11;99(12):7980-5. PMID:12060744[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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